2PKG

Structure of a complex between the A subunit of protein phosphatase 2A and the small t antigen of SV40

2PKG の概要

• エントリーDOI: 10.2210/pdb2pkg/pdb
• 分子名称: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform, Small T antigen, ZINC ION (3 entities in total)
• 機能のキーワード: protein phosphatase 2a, small t antigen, sv40, regulation, hydrolase regulator-viral protein complex, hydrolase regulator/viral protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P30153; Host cytoplasm: P03081
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150279.67

構造登録者

Jeffrey, P.D.,Shi, Y. (登録日: 2007-04-17, 公開日: 2007-05-15, 最終更新日: 2024-02-21)

主引用文献

Chen, Y.,Xu, Y.,Bao, Q.,Xing, Y.,Li, Z.,Lin, Z.,Stock, J.B.,Jeffrey, P.D.,Shi, Y.
Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40.
Nat.Struct.Mol.Biol., 14:527-534, 2007

PubMed Abstract: The small t antigen (ST) of DNA tumor virus SV40 facilitates cellular transformation by disrupting the functions of protein phosphatase 2A (PP2A) through a poorly defined mechanism. The crystal structure of the core domain of SV40 ST bound to the scaffolding subunit of human PP2A reveals that the ST core domain has a novel zinc-binding fold and interacts with the conserved ridge of HEAT repeats 3-6, which overlaps with the binding site for the B' (also called PR61 or B56) regulatory subunit. ST has a lower binding affinity than B' for the PP2A core enzyme. Consequently, ST does not efficiently displace B' from PP2A holoenzymes in vitro. Notably, ST inhibits PP2A phosphatase activity through its N-terminal J domain. These findings suggest that ST may function mainly by inhibiting the phosphatase activity of the PP2A core enzyme, and to a lesser extent by modulating assembly of the PP2A holoenzymes.

PubMed: 17529992
DOI: 10.1038/nsmb1254

実験手法

X-RAY DIFFRACTION (3.3 Å)